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P56716

- RP1_MOUSE

UniProt

P56716 - RP1_MOUSE

Protein

Oxygen-regulated protein 1

Gene

Rp1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 2 (06 Jun 2002)
      Previous versions | rss
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    Functioni

    Microtubule-associated protein regulating the stability and length of the microtubule-based axoneme of photoreceptors. Required for the differentiation of photoreceptor cells, it plays a role in the organization of the outer segment of rod and cone photoreceptors ensuring the correct orientation and higher-order stacking of outer segment disks along the photoreceptor axoneme.2 Publications

    GO - Molecular functioni

    1. microtubule binding Source: UniProtKB

    GO - Biological processi

    1. axoneme assembly Source: UniProtKB
    2. cellular response to light stimulus Source: MGI
    3. intracellular signal transduction Source: InterPro
    4. microtubule polymerization Source: BHF-UCL
    5. negative regulation of microtubule depolymerization Source: BHF-UCL
    6. photoreceptor cell development Source: UniProtKB
    7. photoreceptor cell maintenance Source: UniProtKB
    8. photoreceptor cell outer segment organization Source: UniProtKB
    9. retina development in camera-type eye Source: MGI
    10. retinal cone cell development Source: UniProtKB
    11. retinal rod cell development Source: UniProtKB
    12. retina morphogenesis in camera-type eye Source: MGI
    13. visual perception Source: UniProtKB-KW

    Keywords - Biological processi

    Cilium biogenesis/degradation, Sensory transduction, Vision

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Oxygen-regulated protein 1
    Alternative name(s):
    Retinitis pigmentosa RP1 protein homolog
    Gene namesi
    Name:Rp1
    Synonyms:Orp1, Rp1h
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:1341105. Rp1.

    Subcellular locationi

    Cytoplasmcytoskeletoncilium axoneme. Cell projectionciliumphotoreceptor outer segment
    Note: Specifically localized in the connecting cilia of rod and cone photoreceptors.

    GO - Cellular componenti

    1. axoneme Source: UniProtKB
    2. cilium Source: MGI
    3. microtubule associated complex Source: UniProtKB
    4. photoreceptor connecting cilium Source: UniProtKB
    5. photoreceptor inner segment Source: UniProtKB
    6. photoreceptor outer segment Source: UniProtKB

    Keywords - Cellular componenti

    Cell projection, Cilium, Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Disruption phenotypei

    As early as postnatal day 7, mice have already undergone significant molecular retinal changes. The molecular responses change dramatically during development and were distinct from responses to the disruption of the photoreceptor transcription factors Crx, Pde6b and Nrl. The JNK signaling cascades are specifically compromised in Rp1 defective retinas. Double heterozygotes of Rp1 and Rp1l1 exhibit abnormal outer segment morphology and reduced single rod photosensitivity and dark currents.2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 20952095Oxygen-regulated protein 1PRO_0000097411Add
    BLAST

    Proteomic databases

    PaxDbiP56716.
    PRIDEiP56716.

    PTM databases

    PhosphoSiteiP56716.

    Expressioni

    Tissue specificityi

    Expressed in the cell bodies and inner segments of photoreceptors. Not found in liver, spleen, kidney, brain, thymus, muscle, heart, lung and testis.

    Inductioni

    Gene expression is stimulated by retinal hypoxia and suppressed by relative retinal hyperoxia.

    Gene expression databases

    BgeeiP56716.
    CleanExiMM_RP1H.
    GenevestigatoriP56716.

    Interactioni

    Subunit structurei

    Interacts (via the doublecortin domains) with microtubules. Interacts with RP1L1. Interacts with MAK.3 Publications

    Protein-protein interaction databases

    DIPiDIP-59493N.
    IntActiP56716. 1 interaction.
    MINTiMINT-4132931.
    STRINGi10090.ENSMUSP00000111202.

    Structurei

    3D structure databases

    ProteinModelPortaliP56716.
    SMRiP56716. Positions 34-108.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini35 – 11783Doublecortin 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini157 – 23680Doublecortin 2PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi655 – 6606Poly-Lys

    Domaini

    The doublecortin domains, which mediate interaction with microtubules, are required for regulation of microtubule polymerization and function in photoreceptor differentiation.By similarity

    Sequence similaritiesi

    Contains 2 doublecortin domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG313727.
    GeneTreeiENSGT00530000063898.
    HOGENOMiHOG000136857.
    HOVERGENiHBG018173.
    OMAiEYHMFTH.
    OrthoDBiEOG7N37DH.
    PhylomeDBiP56716.
    TreeFamiTF318770.

    Family and domain databases

    Gene3Di3.10.20.230. 2 hits.
    InterProiIPR003533. Doublecortin_dom.
    [Graphical view]
    PfamiPF03607. DCX. 2 hits.
    [Graphical view]
    SMARTiSM00537. DCX. 2 hits.
    [Graphical view]
    PROSITEiPS50309. DC. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P56716-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSDTPSTSFS MIHLTSEGQV PSPRHSNITH PVVAKRISFY KSGDPQFGGV     50
    RVVVNPRSFK TFDALLDSLS RKVPLPFGVR NISTPRGRHS ITRLEELEDG 100
    KSYVCSHNKK VLPVDLDKAR RRPRPWLSSR SISTHVQLCP ATANMSTMAP 150
    GMLRAPRRLV VFRNGDPKNK HVVLLSRRIT QSFEAFLQYL TQVMQCPVAK 200
    LYATDGRKVP SLQAVILSSG AVVAAGREPF KPGNYDIQKY LLPAKLPGIS 250
    HRVHQKGKAK IEKRKMSTHM PSDLRPQTDS LISEKTYDCF SDFSVAPENY 300
    LALETHESQS LSTYPSEDDV EKSIVFNQDG TMTVVMKVRF KIKEEETVKW 350
    TTTVNRAGLS NNDEKNKKSS YPGKTDYGPS SLKLEACSLP EDIVDTTQQG 400
    SLTEEENTQM TEQQALSCSS ASWENASMET DIQESQKQVK HFYRPPTPGP 450
    RRMRQKKSVI GTVTVVSETE VQEKQFSYSE ERKGGEKSEY HMFTHSCSKM 500
    SSVSNKLVQI GSDNEMESAL ERTRESGSLK SQAINAGAIE ITSQKVLKMC 550
    HNNALPSTAP ENSVVEEGTD NSAVSGTATI KHFRTCGNAN DSFSSITADS 600
    TPTSVNNYSN DRNISELPSV GSPVLTMRLV NEFAHCGLTE KPENRKKVLS 650
    SSASKKKKKK SQQRMITSND KKKVIETKGP PNIAGKIPRA GTTAQERLLQ 700
    ESDCPDKGGR VCEQGLNISP MAIESNNFFP KSNPTFSKNF YKNKLNTFQN 750
    PKTQKLLAKR KSRPRKIVST ERLRKQEIGQ EDKILLHSDS KLCESHLEKQ 800
    SLFHVFNILE EDQKVLHRPP FQVEKVARNL KGMAKKSLVP KVNDLHIMLR 850
    NQKKQMGVKL KSGAEVSEQH VTTRADPLAS LKKPDFPEGI PHHSGKSYVK 900
    RWLQNINSYP DFEHRKSGPL CQNRSDVVNY NRNGFLGNNL HTTSSKGNGF 950
    LMESNKSKTK NDNWSGNTNQ ETGKSLVAKD NGEELNKHHC ESQNGSLYDS 1000
    YLVSLHDNCT LSQTTINEPS TKSHLSIEKS RPEVKLVYQE MNFATKRQSI 1050
    EVAIQVDTMG ENVLKDYLPA LLLRHLEAFV PNNQKHQNGI SQIPGSLAEV 1100
    VFPSVIDNSS TNLLLAWLLV LNLKRTMNSF CQSDAHKMTN RPSETAALLE 1150
    VLKHVAITEE ADDLKAAVAN LMESTKTCSG SSGREQDMLP VNCTASSLHS 1200
    VDECNENGSA QKTLLDEGYS VMGDCTSEMV SKSCNSSCEM HMVSKTNPPK 1250
    QVDDQSDGLL TSNSCTVSQR STGACFLTDG VYSHEACAQK EGVYEGACLS 1300
    DETHIPIRDC HTIHSVHSKE NKCTDDLEST EELKTVDKVP KGLSILADSM 1350
    YKNDSNVSTF QNVNKLSSQR TLLSKTYLDS DKDYSPLEEF QNCPRKKIVN 1400
    KKKSISSDKE ESRTSEEPRS ITNSMTSSER NAISELESFE ELESQDTSIF 1450
    NMNVRAEKKS TKETMQKQSE ARMSSELINV SGRKIIEQER RNTAILETTA 1500
    RGQVTPPSLA FCYDSNKNTE KEISEGETKM RVKKMVDSME NESYSESSLN 1550
    FKKHHRSPGT LDWSDYGSDS ESGYPCKASS NSHNDDSGQE KEPTRGIVKR 1600
    AIEKLYGKAE IIKPPFFHGS IHKSQVCPYN SVEVQCAKKT NFYESECQSL 1650
    VSSEQVSRSS LIFQEFPQVD ANGMGDSFGD SSIENVTKSS AHDRVFTEKE 1700
    NGKLIDNGKW LLRENHLWRV SSDNPGMYGN ADTTSVDTLI DKNSIEVPYS 1750
    HFGELAPGPT MAELSSSEIE EMTQPLEVKC NYFNFPHGSD SEPFGEDFPD 1800
    AQNKTCPKEK IPNHHTEEKG NYPSERLCTS VTQAFVSAGN KVHPVCSDAI 1850
    KTQPLPGSNI THGALQEGDS LDKLYALCGQ HCPILTVIIQ PVNEESRGFA 1900
    YRKDSDIENS LDFQLWMKIY PFMPQSKKHV FRSDGRNVSV GEEFAGNVIG 1950
    DLCDQLYFKS MIDLVDQRAN SLGKEINLKK FQLYLKKSFS DPLSTSLLVV 2000
    ENRNSVSLSP SSWTDNFKSI DENNNFLNRL PNSSKNPNQV VRENTNFQFH 2050
    LELFGQVYLL DICQVEKPLN IKTRSKLEMY YILEGEVLFI WEEEK 2095
    Length:2,095
    Mass (Da):234,388
    Last modified:June 6, 2002 - v2
    Checksum:iCA5301316633BD62
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF155141 mRNA. Translation: AAD42089.2.
    AF291754 Genomic DNA. Translation: AAM17919.1.
    BC120927 mRNA. Translation: AAI20928.1.
    BC120928 mRNA. Translation: AAI20929.1.
    CCDSiCCDS14804.1.
    RefSeqiNP_035413.1. NM_011283.2.
    UniGeneiMm.294263.

    Genome annotation databases

    EnsembliENSMUST00000027032; ENSMUSP00000027032; ENSMUSG00000025900.
    GeneIDi19888.
    KEGGimmu:19888.
    UCSCiuc007aex.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF155141 mRNA. Translation: AAD42089.2 .
    AF291754 Genomic DNA. Translation: AAM17919.1 .
    BC120927 mRNA. Translation: AAI20928.1 .
    BC120928 mRNA. Translation: AAI20929.1 .
    CCDSi CCDS14804.1.
    RefSeqi NP_035413.1. NM_011283.2.
    UniGenei Mm.294263.

    3D structure databases

    ProteinModelPortali P56716.
    SMRi P56716. Positions 34-108.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-59493N.
    IntActi P56716. 1 interaction.
    MINTi MINT-4132931.
    STRINGi 10090.ENSMUSP00000111202.

    PTM databases

    PhosphoSitei P56716.

    Proteomic databases

    PaxDbi P56716.
    PRIDEi P56716.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000027032 ; ENSMUSP00000027032 ; ENSMUSG00000025900 .
    GeneIDi 19888.
    KEGGi mmu:19888.
    UCSCi uc007aex.2. mouse.

    Organism-specific databases

    CTDi 6101.
    MGIi MGI:1341105. Rp1.

    Phylogenomic databases

    eggNOGi NOG313727.
    GeneTreei ENSGT00530000063898.
    HOGENOMi HOG000136857.
    HOVERGENi HBG018173.
    OMAi EYHMFTH.
    OrthoDBi EOG7N37DH.
    PhylomeDBi P56716.
    TreeFami TF318770.

    Miscellaneous databases

    NextBioi 297400.
    PROi P56716.
    SOURCEi Search...

    Gene expression databases

    Bgeei P56716.
    CleanExi MM_RP1H.
    Genevestigatori P56716.

    Family and domain databases

    Gene3Di 3.10.20.230. 2 hits.
    InterProi IPR003533. Doublecortin_dom.
    [Graphical view ]
    Pfami PF03607. DCX. 2 hits.
    [Graphical view ]
    SMARTi SM00537. DCX. 2 hits.
    [Graphical view ]
    PROSITEi PS50309. DC. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Mutations in a gene encoding a new oxygen-regulated photoreceptor protein cause dominant retinitis pigmentosa."
      Pierce E.A., Quinn T., Meehan T., McGee T.L., Berson E.L., Dryja T.P.
      Nat. Genet. 22:248-254(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SEQUENCE REVISION TO 67-76.
      Tissue: Retina.
    2. "Progressive photoreceptor degeneration, outer segment dysplasia, and rhodopsin mislocalization in mice with targeted disruption of the retinitis pigmentosa-1 (Rp1) gene."
      Gao J., Cheon K., Nusinowitz S., Liu Q., Bei D., Atkins K., Azimi A., Daiger S.P., Farber D.B., Heckenlively J.R., Pierce E.A., Sullivan L.S., Zuo J.
      Proc. Natl. Acad. Sci. U.S.A. 99:5698-5703(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 129/Sv.
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. Lubec G., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 357-367, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: OF1.
      Tissue: Hippocampus.
    5. "Identification and subcellular localization of the RP1 protein in human and mouse photoreceptors."
      Liu Q., Zhou J., Daiger S.P., Farber D.B., Heckenlively J.R., Smith J.E., Sullivan L.S., Zuo J., Milam A.H., Pierce E.A.
      Invest. Ophthalmol. Vis. Sci. 43:22-32(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    6. Cited for: FUNCTION, SUBCELLULAR LOCATION.
    7. "The retinitis pigmentosa 1 protein is a photoreceptor microtubule-associated protein."
      Liu Q., Zuo J., Pierce E.A.
      J. Neurosci. 24:6427-6436(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MICROTUBULES, SUBCELLULAR LOCATION.
    8. "Distinct gene expression profiles and reduced JNK signaling in retinitis pigmentosa caused by RP1 mutations."
      Liu J., Huang Q., Higdon J., Liu W., Xie T., Yamashita T., Cheon K., Cheng C., Zuo J.
      Hum. Mol. Genet. 14:2945-2958(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    9. "Essential and synergistic roles of RP1 and RP1L1 in rod photoreceptor axoneme and retinitis pigmentosa."
      Yamashita T., Liu J., Gao J., LeNoue S., Wang C., Kaminoh J., Bowne S.J., Sullivan L.S., Daiger S.P., Zhang K., Fitzgerald M.E., Kefalov V.J., Zuo J.
      J. Neurosci. 29:9748-9760(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RP1L1, DISRUPTION PHENOTYPE.
    10. "Negative regulation of ciliary length by ciliary male germ cell-associated kinase (Mak) is required for retinal photoreceptor survival."
      Omori Y., Chaya T., Katoh K., Kajimura N., Sato S., Muraoka K., Ueno S., Koyasu T., Kondo M., Furukawa T.
      Proc. Natl. Acad. Sci. U.S.A. 107:22671-22676(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAK.

    Entry informationi

    Entry nameiRP1_MOUSE
    AccessioniPrimary (citable) accession number: P56716
    Secondary accession number(s): Q548Q8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: June 6, 2002
    Last modified: October 1, 2014
    This is version 95 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3